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Kinetic and structural changes in hsmtphers, induced by pathogenic mutations in human FARS2

Analyse Kinetic and structural changes in hsmtphers, induced by pathogenic mutations in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5MGV
Type: protein
Length: 405 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Phenylalanine--tRNA ligase, mitochondrial
EC: 6.1.1.20
UniProt: O95363
Pockets: 4 · best druggability 0.68

Structure

x-ray diffraction · 1 distinct chain · 34% helix, 27% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Phenylalanine--tRNA ligase, mitochondrial (EC 6.1.1.20)	protein	405	34% helix, 27% strand	O95363

Pockets

4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	492	0.68	0.79	46	empty
2	120	0.46	0.78	21	empty
3	177	0.42	0.73	22	empty
4	62	0.35	0.77	12	empty

Compared structures

5MGV · Kinetic and Structural Changes in HsmtPheRS, Induced by Pathogenic Mutations in Human… · the same entry in another collection · chain A against A, TM-score 1.00
O95363 · AlphaFold monomer V2.0 prediction for phenylalanine--tRNA ligase, mitochondrial (O95363) · a predicted model of the same protein · chain A against A, TM-score 0.99

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt O95363
Elsewhere: RCSB PDB 5MGV · PDBe 5MGV · UniProt O95363

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